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Concanavalin A-like lectins/glucanases superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All beta proteins [ 48724] (174)
Fold:   Concanavalin A-like lectins/glucanases [ 49898]
Superfamily:   Concanavalin A-like lectins/glucanases [ 49899] (25)
Families:   Legume lectins [ 49900] (4)
  Lectin leg-like [ 74904] (3)
  Glycosyl hydrolases family 16 [ 49925] (5)
  Galectin (animal S-lectin) [ 49932] (8)
  Laminin G-like module [ 49944] (6)
  Thrombospondin C-terminal domain [ 101643]
  Pentraxin (pentaxin) [ 49951] (2)
  Calnexin/calreticulin [ 69236]
  vp4 sialic acid binding domain [ 74907]
  Hypothetical protein YesU [ 101646]
  Alginate lyase [ 101649] (3)
  Clostridium neurotoxins, the second last domain [ 49956] (2)
  Exotoxin A, N-terminal domain [ 49962]
  Vibrio cholerae sialidase, N-terminal and insertion domains [ 49965]
  Leech intramolecular trans-sialidase, N-terminal domain [ 49968]
  Trypanosoma sialidase, C-terminal domain [ 82038]
  Glycosyl hydrolase family 7 catalytic core [ 49971]
  Glycosyl hydrolases family 32 C-terminal domain [ 101652] (2)
  Xylanase/endoglucanase 11/12 [ 49978] (2)
  Peptidase A4 [ 101656] (2)
  Alpha-L-arabinofuranosidase B, N-terminal domain [ 110143]
  SPRY domain [ 141154] (5)
  Beta-D-xylosidase C-terminal domain-like [ 141161]
  SO2946-like [ 141167]
  MAM domain [ 141170]


Superfamily statistics
Genomes (2,197) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 65,045 271,113 236
Proteins 51,285 221,335 228


Functional annotation
General category Metabolism
Detailed category Secondary metabolism

Document:
Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Acting on acid anhydrides1Least InformativeInherited
Enzyme Commission (EC)Acting on peptide bonds (peptide hydrolases)1Least InformativeInherited
Enzyme Commission (EC)Acting on ester bonds1Least InformativeInherited
Enzyme Commission (EC)Protein-serine/threonine kinases0Moderately InformativeDirect
Enzyme Commission (EC)Glycosidases, i.e. enzymes hydrolyzing O- and S-gl0Moderately InformativeDirect
Enzyme Commission (EC)Glycosyltransferases0.000000000002215Moderately InformativeDirect
Enzyme Commission (EC)Acting on acid anhydrides; involved in cellular an0.1378Moderately InformativeInherited
Enzyme Commission (EC)Phosphoric monoester hydrolases0.07915Moderately InformativeInherited
Enzyme Commission (EC)Metalloendopeptidases0InformativeDirect
Enzyme Commission (EC)Protein-tyrosine-phosphatase0.00000001837InformativeDirect
Enzyme Commission (EC)Cellulose 1,4-beta-cellobiosidase (non-reducing en0Highly InformativeDirect
Enzyme Commission (EC)Bontoxilysin0.000000000000213Highly InformativeDirect
Enzyme Commission (EC)Alpha-N-arabinofuranosidase0.0001267Highly InformativeDirect

Document: EC annotation of SCOP domains

Human Phenotype (HP)

(show details)
HP termFDR (all)SDHP levelAnnotation (direct or inherited)
Phenotypic Abnormality (PA)Abnormality of the eye0.1388Least InformativeInherited
Phenotypic Abnormality (PA)Abnormality of limbs0.4166Least InformativeInherited
Phenotypic Abnormality (PA)Abnormality of skeletal morphology0.8097Least InformativeInherited
Phenotypic Abnormality (PA)Abnormality of the thorax0.2452Moderately InformativeInherited
Phenotypic Abnormality (PA)Abnormality of the lower limb0.2783Moderately InformativeInherited
Phenotypic Abnormality (PA)Abnormal globe morphology0.3603Moderately InformativeInherited
Phenotypic Abnormality (PA)Abnormality of limb bone morphology0.8784Moderately InformativeInherited
Phenotypic Abnormality (PA)Abnormal morphology of bones of the lower limbs0.04428InformativeInherited
Phenotypic Abnormality (PA)Abnormal retinal morphology0.2226InformativeInherited
Phenotypic Abnormality (PA)Abnormality of long bone morphology0.5361InformativeInherited
Phenotypic Abnormality (PA)Abnormality of femoral epiphysis0.0000409Highly InformativeDirect
Phenotypic Abnormality (PA)Abnormality of the ribs0.2168Highly InformativeInherited

Document: HP annotation of SCOP domains

Mouse Phenotype (MP)

(show details)
MP termFDR (all)SDMP levelAnnotation (direct or inherited)
Mammalian Phenotype (MP)nervous system phenotype0.02392Least InformativeInherited
Mammalian Phenotype (MP)cellular phenotype0.8891Least InformativeInherited
Mammalian Phenotype (MP)abnormal nervous system development0.3743Moderately InformativeInherited
Mammalian Phenotype (MP)abnormal nervous system physiology0.8143Moderately InformativeInherited
Mammalian Phenotype (MP)abnormal spinal cord morphology0.5018InformativeInherited
Mammalian Phenotype (MP)abnormal spinal cord ventral commissure morphology0.0002289Highly InformativeDirect
Mammalian Phenotype (MP)abnormal basement membrane morphology0.0005222Highly InformativeDirect

Document: MP annotation of SCOP domains

Worm Phenotype (WP)

(show details)
WP termFDR (all)SDWP levelAnnotation (direct or inherited)
Worm Phenotype (WP)cell development variant0.08972Least InformativeInherited
Worm Phenotype (WP)organ system morphology variant0.1058Least InformativeInherited
Worm Phenotype (WP)cell morphology variant0.1793Least InformativeInherited
Worm Phenotype (WP)nervous system morphology variant0.007451Moderately InformativeInherited
Worm Phenotype (WP)neurite morphology variant0.00001497InformativeDirect
Worm Phenotype (WP)axon outgrowth variant0.0003111InformativeDirect
Worm Phenotype (WP)axon guidance variant0.00002091Highly InformativeDirect
Worm Phenotype (WP)cell polarity variant0.0007121Highly InformativeDirect
Worm Phenotype (WP)myopodia present0.000781Highly InformativeDirect
Worm Phenotype (WP)muscle arm development defective0.0009889Highly InformativeDirect
Worm Phenotype (WP)axon trajectory variant0.2219Highly InformativeInherited

Document: WP annotation of SCOP domains

Yeast Phenotype (YP)

(show details) Document: YP annotation of SCOP domains

Fly Phenotype (FP)

(show details)
FP termFDR (all)SDFP levelAnnotation (direct or inherited)
Fly Phenotype (FP)cell polarity defective0.00004714InformativeDirect

Document: FP annotation of SCOP domains

Fly Anatomy (FA)

(show details) Document: FA annotation of SCOP domains

Zebrafish Anatomy (ZA)

(show details)
ZA termFDR (all)SDZA levelAnnotation (direct or inherited)
Zebrafish Anatomy (ZA)organism subdivision0.9173Least InformativeInherited
Zebrafish Anatomy (ZA)portion of tissue0.006854Moderately InformativeInherited
Zebrafish Anatomy (ZA)surface structure0.7999InformativeInherited
Zebrafish Anatomy (ZA)integument0.2461Highly InformativeInherited
Zebrafish Anatomy (ZA)epithelium0.5776Highly InformativeInherited

Document: ZA annotation of SCOP domains

Xenopus Anatomy (XA)

(show details) Document: XA annotation of SCOP domains

Arabidopsis Plant Ontology (AP)

(show details)
AP termFDR (all)SDAP levelAnnotation (direct or inherited)
Plant ANatomical entity (PAN)root system0.4785Least InformativeInherited
Plant ANatomical entity (PAN)leaf0.8409Least InformativeInherited
Plant ANatomical entity (PAN)root epidermis0.001718InformativeInherited
Plant ANatomical entity (PAN)adult vascular leaf0.0007043Highly InformativeDirect

Document: AP annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Hydrolases0Least InformativeDirect
Enzyme Commission (EC)Transferring phosphorus-containing groups1Least InformativeInherited
Enzyme Commission (EC)Aminoacyltransferases0Moderately InformativeDirect
Enzyme Commission (EC)Glycosylases0Moderately InformativeDirect
Enzyme Commission (EC)Protein-serine/threonine kinases0.00000000000004585Moderately InformativeDirect
Enzyme Commission (EC)Glycosyltransferases0.000000324Moderately InformativeDirect
Enzyme Commission (EC)Phosphoric monoester hydrolases0.3789Moderately InformativeInherited
Enzyme Commission (EC)Acting on peptide bonds (peptidases)1Moderately InformativeInherited
Enzyme Commission (EC)RING-type E3 ubiquitin transferase0InformativeDirect
Enzyme Commission (EC)Hexosyltransferases0InformativeDirect
Enzyme Commission (EC)Non-specific serine/threonine protein kinase0InformativeDirect
Enzyme Commission (EC)Metalloendopeptidases0InformativeDirect
Enzyme Commission (EC)Protein-tyrosine-phosphatase0.0000003645InformativeDirect
Enzyme Commission (EC)Serine endopeptidases1InformativeInherited

Document: EC annotation of SCOP domains

InterPro annotation
Cross references IPR008985 SSF49899 Protein matches
Abstract

Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain, which consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse, and include the lectins: legume lectins, cereal lectins, viral lectins, and animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds, the binding of nitrogen-fixing bacteria to root hairs, the inhibition of fungal growth or insect feeding, and in hormonally regulated plant growth [PubMed9094437]. Protein members include concanavalin A (Con A), favin, isolectin I, lectin IV, soybean agglutinin and lentil lectin. Animal lectins include the galectins, which are S-type lactose-binding and IgE-binding proteins such as S-lectin, CLC protein, galectin1, galectin2, galectin3 CRD, and Congerin I [PubMed11834744].

Other members with a Con A-like domain include the glucanases and xylanases. Bacterial and fungal beta-glucanases, such as Bacillus 1-3,1-4-beta-glucanse, carry out the acid catalysis of beta-glucans found in microorganisms and plants [PubMed7589539]. Similarly, kappa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls [PubMed11435116]. Xylanase and cellobiohydrolase I degrade hemicellulose and cellulose, respectively [PubMed9618460, PubMed9466911].

There are many Con A-like domains found in proteins involved in cell recognition and adhesion. For example, several viral and bacterial toxins carry Con A-like domains. Examples include the Clostridium neurotoxins responsible for the neuroparalytic effects of botulism and tetanus [PubMed10932256]. The Pseudomonas exotoxin A, a virulence factor which is highly toxic to eukaryotic cells, causing the arrest of protein synthesis, contains a Con A-like domain involved in receptor binding [PubMed11734000]. Cholerae neuraminidase can bind to cell surfaces, possibly through their Con A-like domains, where they function as part of a mucinase complex to degrade the mucin layer of the gastrointestinal tract [PubMed7922030]. The rotaviral outer capsid protein, VP4, has a Con A-like sialic acid binding domain, which functions in cell attachment and membrane penetration [PubMed11867517].

Con A-like domains also play a role in cell recognition in eukaryotes. Proteins containing a Con A-like domain include the sex hormone-binding globulins which transport sex steroids in blood and regulate their access to target tissues [PubMed10675319], laminins which are large heterotrimeric glycoproteins involved in basement membrane architecture and function [PubMed10747011], neurexins which are expressed in hundreds of isoforms on the neuronal cell surface, where they may function as cell recognition molecules [PubMed10520997] and sialidases that are found in both microorganisms and animals, and function in cell adhesion and signal transduction [PubMed12419220].

Other proteins containing a Con A-like domain include pentraxins and calnexins. The pentraxin PTX3 is a TNFalpha-induced, secreted protein of adipose cells produced during inflammation [PubMed12611905]. The calnexin family of molecular chaperones is conserved among plants, fungi, and animals. Family members include Calnexin, a type-I integral membrane protein in the endoplasmic reticulum which coordinates the processing of newly synthesized N-linked glycoproteins with their productive folding, calmegin, a type-I membrane protein expressed mainly in the spermatids of the testis, and calreticulin, a soluble ER lumenal paralog [PubMed11583625].


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Human Phenotype (HP) · Mouse Phenotype (MP) · Worm Phenotype (WP) · Yeast Phenotype (YP) · Fly Phenotype (FP) · Fly Anatomy (FA) · Zebrafish Anatomy (ZA) · Xenopus Anatomy (XA) · Arabidopsis Plant Ontology (AP) · Enzyme Commission (EC) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 121 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a Concanavalin A-like lectins/glucanases domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 121 hidden Markov models representing the Concanavalin A-like lectins/glucanases superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Human Phenotype (HP) · Mouse Phenotype (MP) · Worm Phenotype (WP) · Yeast Phenotype (YP) · Fly Phenotype (FP) · Fly Anatomy (FA) · Zebrafish Anatomy (ZA) · Xenopus Anatomy (XA) · Arabidopsis Plant Ontology (AP) · Enzyme Commission (EC) · Internal database links ]